Mathematical modeling of intracellular transport processes and the creatine kinase systems: a probability approach

1994 ◽  
Vol 133-134 (1) ◽  
pp. 333-346 ◽  
Author(s):  
M. K. Aliev ◽  
V. A. Saks
Keyword(s):  
Mathematical Modeling ◽  
Creatine Kinase ◽  
Intracellular Transport ◽  
Transport Processes ◽  
Probability Approach

scholarly journals Role of the Guanine Nucleotide Exchange Factor GBF1 in the Replication of RNA Viruses

Viruses ◽  
2020 ◽  
Vol 12 (6) ◽  
pp. 682
Author(s):  
José L. Martínez ◽  
Carlos F. Arias
Keyword(s):  
Intracellular Transport ◽  
Rna Viruses ◽  
Guanine Nucleotide Exchange Factor ◽  
Transport Processes ◽  
Guanine Nucleotide ◽  
Nucleotide Exchange ◽  
Intracellular Traffic ◽  
Exchange Factor ◽  
Guanine Nucleotide Exchange ◽  
Nucleotide Exchange Factor

The guanine nucleotide exchange factor GBF1 is a well-known factor that can activate different ADP-ribosylation factor (Arf) proteins during the regulation of different cellular vesicular transport processes. In the last decade, it has become increasingly evident that GBF1 can also regulate different steps of the replication cycle of RNA viruses belonging to different virus families. GBF1 has been shown not only to facilitate the intracellular traffic of different viral and cellular elements during infection, but also to modulate the replication of viral RNA, the formation and maturation of viral replication complexes, and the processing of viral proteins through mechanisms that do not depend on its canonical role in intracellular transport. Here, we review the various roles that GBF1 plays during the replication of different RNA viruses.

Mathematical Modeling of the Unit Load Formation

2013 ◽  
Vol 309 ◽  
pp. 358-365 ◽  
Author(s):  
Béla Illés ◽  
Gabriella Bognár
Keyword(s):  
Mathematical Modeling ◽  
Supply Chain ◽  
Significant Role ◽  
Mathematical Description ◽  
Raw Materials ◽  
Transport Processes ◽  
Optimization Process ◽  
Objective Functions ◽  
Unit Load ◽  
Major Factors

A fast and efficient way of handling and storing components, raw materials, semi-finished and finished products play a significant role in the development of transport, storage and distribution design within the supply chain. One of the most important issues in storage and transport processes is the formation of unit loads. Our main goal is to give a mathematical description of a model involving the major factors of the unit load formation. The optimization process is exhibited applying the determined objective functions and constraints related to the basic tasks.

Thyroid control over membrane processes in rat heart

1991 ◽  
Vol 261 (4) ◽  
pp. L66-L71
Author(s):  
Enn K. Seppet ◽  
Lumme Y. Kadaya ◽  
Tomoji Hata ◽  
Ants P. Kallikorm ◽  
Valdur A. Saks ◽  
...  
Keyword(s):  
Creatine Kinase ◽  
Oxidative Phosphorylation ◽  
Atpase Activity ◽  
Rat Heart ◽  
Transport Processes ◽  
Functional Coupling ◽  
Mitochondrial Creatine Kinase ◽  
Thyroid State ◽  
Hyperthyroid Heart ◽  
Pumping Activity

We have studied the effects of hypo- and hyperthyroidism on sarcolemmal (SL) and sarcoplasmic reticular (SR) ion transport processes and mitochondrial energy production in rat heart. The following conclusions were derived. 1) Compared with euthyroid state, hyperthyroidism led to increased SR Ca+-accumulation. In SL, the activities of Ca2+-stimulated adenosine triphosphatase (ATPase), ATP-dependent Ca+ pumping, and Na+-Ca2+ exchanger were not affected; but ouabain-sensitive Na+-K+-ATPase activity was enhanced. 2) Hypothyroidism resulted in depressed activities of Ca2+ pumps both in SL and SR. In SL, the Na+-K+-ATPase activity was decreased, but Na+-Ca2+ exchange was unaltered. 3) Thus slower relaxation of the hypothyroid myocardium may be attributed to depressed functioning of Ca2+ pumps in SR and SL, whereas faster relaxation of the hyperthyroid heart may be based on increased Ca2+-pumping activity of SR. 4) Hyperthyroidism and hypothyroidism, respectively, led to enhanced and decreased rates of mitochondrial phosphocreatine synthesis. The thyroid state appears to control the functional coupling between mitochondrial creatine kinase and ATP-ADP translocase: the energy of oxidative phosphorylation was transformed into phosphocreatine more effectively in mitochondria from hypothyroid hearts than in those from hyperthyroid hearts. euthyroid; hyperthyroid; hypothyroid; mitochondrial creatine kinase; myocardium; oxidative phosphorylation; phosphocreatine synthesis; sarcolemma; sarcoplasmic reticulum

Investigation of processes occurring at cathodically protected underground installations: Mathematical modeling of reaction transport processes in soil

2017 ◽  
Vol 120 ◽  
pp. 28-41 ◽  
Author(s):  
Roman Kodým ◽  
Dalimil Šnita ◽  
Vlastimil Fíla ◽  
Karel Bouzek ◽  
Milan Kouřil
Keyword(s):  
Mathematical Modeling ◽  
Transport Processes ◽  
Reaction Transport

Cytoplasmic Dynein Function Is Essential in Drosophila melanogaster

Genetics ◽  
1996 ◽  
Vol 142 (3) ◽  
pp. 865-878 ◽  
Author(s):  
Janice Gepner ◽  
Min-gang Li ◽  
Susan Ludmann ◽  
Cynthia Kortas ◽  
Kristin Boylan ◽  
...  
Keyword(s):  
Heavy Chain ◽  
Intracellular Transport ◽  
Mutational Analysis ◽  
Cytoplasmic Dynein ◽  
Complementation Group ◽  
Transport Processes ◽  
Female Sterility ◽  
Chain Gene ◽  
Heavy Chain Gene ◽  
Dynein Heavy Chain

Abstract The microtubule motor cytoplasmic dynein has been implicated in a variety of intracellular transport processes. We previously identified and characterized the Drosophila gene Dhc64C, which encodes a cytoplasmic dynein heavy chain. To investigate the function of the cytoplasmic dynein motor, we initiated a mutational analysis of the Dhc64C dynein gene. A small deletion that removes the chromosomal region containing the heavy chain gene was used to isolate EMS-induced lethal mutations that define at least eight essential genes in the region. Germline transformation with a Dhc64C transgene rescued 16 mutant alleles in the single complementation group that identifies the dynein heavy chain gene. All 16 alleles were hemizygous lethal, which demonstrates that the cytoplasmic dynein heavy chain gene Dhc64C is essential for Drosophila development. Furthermore, our failure to recover somatic clones of cells homozygous for a Dhc64C mutation indicates that cytoplasmic dynein function is required for cell viability in several Drosophila tissues. The intragenic complementation of dynein alleles reveals multiple mutant phenotypes including male and/or female sterility, bristle defects, and defects in eye development.

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